Mediator head subcomplex Med11/22 contains a common helix bundle building block 
with a specific function in transcription initiation complex stabilization

Seizl, M.; Larivière, L.; Pfaffeneder, T.; Wenzeck, L.; Cramer, P.

doi:10.1093/nar/gkr229

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Mediator head subcomplex Med11/22 contains a common helix bundle building block with a specific function in transcription initiation complex stabilization

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Cramer, P.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Citation

Seizl, M., Larivière, L., Pfaffeneder, T., Wenzeck, L., & Cramer, P. (2011). Mediator head subcomplex Med11/22 contains a common helix bundle building block with a specific function in transcription initiation complex stabilization. Nucleic Acids Research, 39(14), 6291-6304. doi:10.1093/nar/gkr229.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0015-7F99-3

Abstract

Mediator is a multiprotein co-activator of RNA polymerase (Pol) II transcription. Mediator contains a conserved core that comprises the ‘head’ and ‘middle’ modules. We present here a structure– function analysis of the essential Med11/22 heterodimer, a part of the head module. Med11/22 forms a conserved four-helix bundle domain with C-terminal extensions, which bind the central head subunit Med17. A highly conserved patch on the bundle surface is required for stable transcription preinitiation complex formation on a Pol II promoter in vitro and in vivo and may recruit the general transcription factor TFIIH. The bundle domain fold is also present in the Mediator middle module subcomplex Med7/21 and is predicted in the Mediator heterodimers Med2/3, Med4/9, Med10/14 and Med28/30. The bundle domain thus represents a common building block that has been multiplied and functionally diversified during Mediator evolution in eukaryotes.